We are grateful to J. Bernhagen for helpful discussions and to K. Alexandrov and R. S. Goody for help with analysis of fluorescence data. We thank A. Kazantzis, K. Tenidis, M. Waldner, H. Vasen, and M. Müsken for peptide synthesis and D. Bächle, PANATecs GmbH, R. Fischer, and H. Kalbacher for MALDI measurements. This work was supported in part by the Deutsche Forschungsgemeinschaft (DFG). Aβ=β-amyloid peptide; IAPP=islet amyloid polypeptide.
Communication
IAPP Mimic Blocks Aβ Cytotoxic Self-Assembly: Cross-Suppression of Amyloid Toxicity of Aβ and IAPP Suggests a Molecular Link between Alzheimer's Disease and Type II Diabetes†
Article first published online: 4 JAN 2007
DOI: 10.1002/anie.200604056
Copyright © 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Yan, L.-M., Velkova, A., Tatarek-Nossol, M., Andreetto, E. and Kapurniotu, A. (2007), IAPP Mimic Blocks Aβ Cytotoxic Self-Assembly: Cross-Suppression of Amyloid Toxicity of Aβ and IAPP Suggests a Molecular Link between Alzheimer's Disease and Type II Diabetes. Angew. Chem. Int. Ed., 46: 1246–1252. doi: 10.1002/anie.200604056
- †
Publication History
- Issue published online: 5 FEB 2007
- Article first published online: 4 JAN 2007
- Manuscript Received: 3 OCT 2006
Funded by
- Deutsche Forschungsgemeinschaft
Keywords:
- β-amyloids;
- Alzheimer's disease;
- amyloid fibrils;
- protein design;
- self-assembly

Le fabuleux destin d'amyloid disease: A peptide-derived inhibitor for amyloid diseases binds the Alzheimer's disease β-amyloid peptide (Aβ40) and the type II diabetes islet amyloid polypeptide (IAPP) and blocks cytotoxic self-assembly of both peptides. Evidence is also presented for a high-affinity interaction between Aβ40 and IAPP that results in cross-suppression of cytotoxic self-association of both peptides.

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